4OH4

Crystal structure of BRI1 in complex with BKI1

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004672	molecular_function	protein kinase activity
A	0005524	molecular_function	ATP binding
A	0006468	biological_process	protein phosphorylation
B	0004672	molecular_function	protein kinase activity
B	0005524	molecular_function	ATP binding
B	0006468	biological_process	protein phosphorylation

Functional Information from PDB Data

site_id	AC1
Number of Residues	15
Details	BINDING SITE FOR RESIDUE ANP A 1201

Chain	Residue
A	GLY893
A	LYS1011
A	SER1013
A	ASN1014
A	LEU1016
A	ASP1027
A	HOH1420
A	ALA909
A	LYS911
A	TYR956
A	GLU957
A	PHE958
A	MET959
A	SER963
A	ASP966

---

site_id	AC2
Number of Residues	21
Details	BINDING SITE FOR RESIDUE ANP B 1201

Chain	Residue
B	ILE889
B	SER891
B	GLY892
B	GLY893
B	VAL897
B	ALA909
B	LYS911
B	TYR956
B	GLU957
B	PHE958
B	MET959
B	SER963
B	ASP966
B	LYS1011
B	SER1013
B	ASN1014
B	LEU1016
B	ASP1027
B	HOH1322
B	HOH1343
B	HOH1383

---

Functional Information from PROSITE/UniProt

site_id	PS00107
Number of Residues	24
Details	PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGSGGFGDVYkAilkdgsav..........AIKK

Chain	Residue	Details
A	ILE889-LYS912

---

site_id	PS00108
Number of Residues	13
Details	PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IiHrDMKssNVLL

Chain	Residue	Details
A	ILE1005-LEU1017

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027

Chain	Residue	Details
A	ASP1009
B	ASP1009

---

site_id	SWS_FT_FI2
Number of Residues	2
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159

Chain	Residue	Details
A	ILE889
B	ILE889

---

site_id	SWS_FT_FI3
Number of Residues	10
Details	BINDING: BINDING => ECO:0000269|PubMed:24461462

Chain	Residue	Details
A	LYS911
B	ASP1027
A	GLU957
A	SER963
A	ASP1009
A	ASP1027
B	LYS911
B	GLU957
B	SER963
B	ASP1009

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	MOD_RES: Phosphothreonine => ECO:0000269|PubMed:11027724, ECO:0000269|PubMed:15894717

Chain	Residue	Details
A	THR872
B	THR872

---

site_id	SWS_FT_FI5
Number of Residues	4
Details	MOD_RES: Phosphothreonine => ECO:0000269|PubMed:15894717

Chain	Residue	Details
A	THR880
A	THR982
B	THR880
B	THR982

---

site_id	SWS_FT_FI6
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0000269|PubMed:19105183

Chain	Residue	Details
A	SER887
B	SER887

---

site_id	SWS_FT_FI7
Number of Residues	12
Details	MOD_RES: Phosphoserine => ECO:0000255

Chain	Residue	Details
A	SER891
B	SEP1042
B	SEP1060
B	SER1172
A	SER981
A	SER1035
A	SEP1042
A	SEP1060
A	SER1172
B	SER891
B	SER981
B	SER1035

---

site_id	SWS_FT_FI8
Number of Residues	2
Details	MOD_RES: Phosphotyrosine => ECO:0000269|PubMed:19124768

Chain	Residue	Details
A	TYR956
B	TYR956

---

site_id	SWS_FT_FI9
Number of Residues	8
Details	MOD_RES: Phosphothreonine => ECO:0000255

Chain	Residue	Details
A	TPO1039
A	THR1045
A	THR1049
A	THR1169
B	TPO1039
B	THR1045
B	THR1049
B	THR1169

---

site_id	SWS_FT_FI10
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q9M0G7, ECO:0000255

Chain	Residue	Details
A	SEP1044
B	SEP1044

---

site_id	SWS_FT_FI11
Number of Residues	2
Details	MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:C0LGT6

Chain	Residue	Details
A	TYR1052
B	TYR1052

---

site_id	SWS_FT_FI12
Number of Residues	2
Details	MOD_RES: Phosphotyrosine => ECO:0000255

Chain	Residue	Details
A	TYR1072
B	TYR1072

---

site_id	SWS_FT_FI13
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0000269|PubMed:18694562

Chain	Residue	Details
A	SER1166
B	SER1166

---

site_id	SWS_FT_FI14
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0000269|PubMed:15894717

Chain	Residue	Details
A	SER1168
B	SER1168

---